Kyushu University Academic Staff Educational and Research Activities Database
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Nobuaki Matsumori Last modified date:2018.06.21

Professor / Inorganic Chemistry and Analytical Chemistry
Department of Chemistry
Faculty of Sciences


Graduate School
Undergraduate School


E-Mail
Homepage
http://www.scc.kyushu-u.ac.jp/BioanalChem/index.html
Department of Chemistry, Kyushu University, Latoratory of Bioanalytical Chemistry
.
Phone
092-802-4153
Fax
092-802-4153
Academic Degree
Doctor of Science
Country of degree conferring institution (Overseas)
No
Field of Specialization
Bioanalytical chemistry, Chemical biology, Natural products chemistry
ORCID(Open Researcher and Contributor ID)
0000-0003-0495-2044
Total Priod of education and research career in the foreign country
01years00months
Outline Activities
To totally understand biomembranes including membrane proteins, we performed integrated analyses of membranes by using various methods of not only analytical chemistry but also organic chemistry, chemical biology, and structure biology. In more detail, we are studying lipid rafts and lipid diversity for the basic understanding of biomembranes, and mechanism of action of membrane-acting drugs such as anesthetics.
Research
Research Interests
  • Bioanalytical chemistry
    keyword : biomembranes, bioanalysis
    2014.07~2024.12.
Academic Activities
Papers
1. Masanao Kinoshita, Kenichi G.N. Suzuki, Nobuaki Matsumori, Misa Takada, Hikaru Ano, Kenichi Morigaki, Mitsuhiro Abe, Asami Makino, Toshihide Kobayashi, Koichiro M. Hirosawa, Takahiro K. Fujiwara, Akihiro Kusumi, Michio Murata, Raft-based sphingomyelin interactions revealed by new fluorescent sphingomyelin analogs, Journal of Cell Biology, 10.1083/jcb.201607086, 216, 4, 1183-1204, 2017.04, Sphingomyelin (SM) has been proposed to form cholesterol-dependent raft domains and sphingolipid domains in the plasma membrane (PM). How SM contributes to the formation and function of these domains remains unknown, primarily because of the scarcity of suitable fluorescent SM analogs. We developed new fluorescent SM analogs by conjugating a hydrophilic fluorophore to the SM choline headgroup without eliminating its positive charge, via a hydrophilic nonaethylene glycol linker. The new analogs behaved similarly to the native SM in terms of their partitioning behaviors in artificial liquid order-disorder phase-separated membranes and detergent-resistant PM preparations. Single fluorescent molecule tracking in the live-cell PM revealed that they indirectly interact with each other in cholesterol- and sphingosine backbone-dependent manners, and that, for ~10-50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size-, cholesterol-, and GPI anchoring-dependent manners. These results suggest that SM continually and rapidly exchanges between CD59-associated raft domains and the bulk PM..
2. 松森 信明, Detailed Comparison of Deuterium Quadrupole Profiles between Sphingomyelin and Phosphatidylcholine Bilayers, BIOPHYSICAL JOURNAL, 10.1016/j.bpj.2013.12.034, 106, 3, 631-638, 2014.02.
Presentations
1. 松森 信明, Small molecule interactions with membrane sterol, Pacifichem2015, 2015.12.
2. 松森 信明, NMR studies of lipid rafts, Pacifichem2015, 2015.12.
Membership in Academic Society
  • Biophysical Society
  • American Chemical Society
  • Chemical Society of Japan
Awards
  • Stereochemical determination of acyclic natural products on the basis of long-range C-H spin coupling constants
Educational
Educational Activities
Chemistry in Daily Life
Analytical Chemistry I
Advanced Analytical Chemistry II
Analytical Chemistry III
Analytical Chemistry Experiment